Poster Presentation The 42nd Lorne Conference on Protein Structure and Function 2017

Controlling the oligomerization of Human Peroxiredoxin 3 for use in bionanotechnology  (#128)

Frankie L. Conroy 1 , N. Amy Yewdall 1 2 , Laura J. Domigan 1 , Alok K. Mitra 1 , Juliet A. Gerrard 1 3 4 5
  1. School of biological sciences , University of Auckland, Auckland Central , Auckland, New Zealand
  2. Biomolecular interaction center and school of biological sciences , University of Canterbury , Christchurch, New Zealand
  3. MacDiarmid Institute for Advanced Materials and Nanotechnology, Victoria University , Wellington, New Zealand
  4. School of Chemical Sciences, University of Auckland , Auckland , New Zealand
  5. Callaghan Innovation Research Limited, Lower Hutt, New Zealand

Bionanotechnology offers opportunities to simplify the production of, and produce biocompatible, nanotechnologies. Recent years have seen biology’s vast range of self-assembling structures and functionalities being translated into usable technologies; it is this work we want to build upon. Proteins naturally cover a vast landscape of structures, functions, and complexities. While this makes them difficult to manipulate relative to DNA and RNA based biotechnology, their higher level of functional complexity makes them an ideal candidate for development as next generation biomaterials [1]. The structural control of proteins is a key step in utilizing this resource as a technology. If we can control the oligomeric state proteins assemble into under various conditions, then we can produce proteins that will self-assemble into structures desired for a range of uses. One attractive protein in this regard is Human Peroxiredoxin 3, which can form dimers, rings, and stacks in a controllable manner and in response to multiple environmental stimuli, including pH and redox conditions [2]. I have explored these changes using rational mutations to increase the control over the oligomerization of this protein; designing mutations that affect the protein's ability to stack, the size of the ring, and searching for greater control over when and how the protein assembles into these higher molecular weight structures. Also key to developing nanotechnologies is the tools we have to examine the structures produced. I have thus also explored aspects of transmission electron microscopy that will allow us to better and more accurately visualize protein nanostructures.

  1. [1] Luo, Q., Hou, C., Bai, Y., Wang, R., & Liu, J. (2016). Protein Assembly: Versatile Approaches to Construct Highly Ordered Nanostructures. Chemical Reviews.
  2. [2] Yewdall, N. A., Venugopal, H., Desfosses, A., Abrishami, V., Yosaatmadja, Y., Hampton, M., Gerrard, J., Goldstone, D., Mitra, A., Radjainia, M. (2016). Structures of Human Peroxiredoxin 3 Suggest Self-Chaperoning Assembly that Maintains Catalytic State. Structure, 24(7), 1120–1129.